Unfortunately due to lack of commercial feasibility, the SkyBLAST service has been suspended from December 1st, 2025.
All subscriptions for paid accounts have been paused. For further information or enquiries, please email [email protected]
LOCUS WP_005302486 291 aa linear BCT 19-FEB-2025 ACCESSION WP_005302486 VERSION WP_005302486.1 KEYWORDS RefSeq. SOURCE Photobacterium damselae ORGANISM Photobacterium damselae Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae; Photobacterium. REFERENCE 1 (residues 1 to 291) AUTHORS Brzezinski,P. and Larsson,G. TITLE Redox-driven proton pumping by heme-copper oxidases JOURNAL Biochim Biophys Acta 1605 (1-3), 1-13 (2003) PUBMED 12907296 REFERENCE 2 (residues 1 to 291) AUTHORS Michel,H. TITLE Cytochrome c oxidase: catalytic cycle and mechanisms of proton pumping--a discussion JOURNAL Biochemistry 38 (46), 15129-15140 (1999) PUBMED 10563795 REFERENCE 3 (residues 1 to 291) AUTHORS Garcia-Horsman,J.A., Barquera,B., Rumbley,J., Ma,J. and Gennis,R.B. TITLE The superfamily of heme-copper respiratory oxidases JOURNAL J Bacteriol 176 (18), 5587-5600 (1994) PUBMED 8083153 COMMENT REFSEQ: This record represents a single, non-redundant, protein sequence which may be annotated on many different RefSeq genomes from the same, or different, species. ##Evidence-For-Name-Assignment-START## Evidence Category :: Conserved Domain (CDD) Evidence Accession :: Domain architecture ID 10108868 Evidence Source :: NCBI SPARCLE ##Evidence-For-Name-Assignment-END## COMPLETENESS: full length. FEATURES Location/Qualifiers source 1..291 /organism="Photobacterium damselae" /db_xref="taxon:38293" Protein 1..291 /product="cytochrome c oxidase subunit 3" /EC_number="7.1.1.9" /GO_function="GO:0004129 - cytochrome-c oxidase activity [Evidence IEA]" /GO_function="GO:0009055 - electron transfer activity [Evidence IEA]" /GO_process="GO:0009060 - aerobic respiration [Evidence IEA]" /GO_process="GO:0019646 - aerobic electron transport chain [Evidence IEA]" /calculated_mol_wt=32560 Region 20..290 /region_name="Cyt_c_Oxidase_III" /note="Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the respiratory chains of eukaryotes and most bacteria, is a multi-chain transmembrane protein located in the inner membrane of mitochondria and the cell membrane of...; cd01665" /db_xref="CDD:238834" Site order(62,65..66,69,72..73) /site_type="other" /note="Subunit III/VIIa interface [polypeptide binding]" /db_xref="CDD:238834" Site order(63..64,67..68,71,76,87..88,91,246,253,265..266) /site_type="other" /note="Phospholipid binding site [chemical binding]" /db_xref="CDD:238834" Site order(79,82..83,94,97,101..102,108,223..224,227,231) /site_type="other" /note="Subunit I/III interface [polypeptide binding]" /db_xref="CDD:238834" Site 141 /site_type="other" /note="Subunit III/VIb interface [polypeptide binding]" /db_xref="CDD:238834" Site order(155..157,174,200,210..212,221..223) /site_type="other" /note="Subunit III/VIa interface" /db_xref="CDD:238834" Site 186 /site_type="other" /note="Subunit III/Vb interface [polypeptide binding]" /db_xref="CDD:238834" ORIGIN 1 mdkspqqpsy yvpdssiwpi vgavalflia lgagttvgnl lagngpwill tglgilliml 61 fgwfrdviie smqglyssql drsfrqgmsw fifsevmffv affgalfyar miavpwlgga 121 snnamthavl wpdfvaiwpl ettpdgrttq amgplglply ntlilltssv tihiahmame 181 qnrrprvilf llltvllgal fvylqgveyl hayqemgltl dagiygntff mltgfhglhv 241 tlgavllfiv wcrvmmghfs ahkhfafqag vwywhfvdvv wlclfvfvyi l